The pilus extrusion/DNA uptake system of Thermus thermophilus contains a 13-mer of the 757-residue PilQ protein and a tightly bound protein outside the outer membrane with a role in DNA binding.
Electron cryo-tomography reveals a huge conformational change in the secretin domain of the type IV pilus machinery that occurs when the channel opens for pilus extrusion.
The dynamic structure of respiratory complex I from mesophilic bacterium is revealed and demonstrates existence of uncoupled conformations in the bacterial complex.
Kristian Parey, Ulrich Brandt ... Volker Zickermann
The site of ubiquinone binding observed in the cryo-EM structure of respiratory complex I during turnover supports a two-state stabilization change mechanism.
The cyclic-peptide antibiotic GE23077 inhibits bacterial RNA polymerase through a novel target that exhibits low susceptibility to target-based resistance and that enables synthesis of bipartite inhibitors that are exceptionally potent and refractory to target-based resistance.
Chemical modifications near the tRNA anticodon and specific mRNA–tRNA pairs combine to control the ribosomal three-nucleotide mRNA reading frame, essential for the sequential addition of amino acids into polypeptide chains.
Oliver W Bayfield, Alasdair C Steven, Alfred A Antson
Structure of the portal protein of a thermostable virus, determined in its capsid-bound state, reveals a molecular mechanism that prevents DNA slippage during genome packaging.
Minimal changes allow an ancestral, unfolded peptide to adopt a known fold by repetition, illuminating a possible path for the emergence of folded proteins at the origin of life.
The crystal structure of Thermus transcription activation complexes containing the transcriptional activator CarD reveals a new mechanism for the activation of transcription.